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  • 1
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    Chromosome dynamics in the yeast interphase nucleus (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-12
    Description: Little is known about the dynamics of chromosomes in interphase nuclei. By tagging four chromosomal regions with a green fluorescent protein fusion to lac repressor, we monitored the movement and subnuclear position of specific sites in the yeast genome, sampling at short time intervals. We found that early and late origins of replication are highly mobile in G1 phase, frequently moving at or faster than 0.5 micrometers/10 seconds, in an energy-dependent fashion. The rapid diffusive movement of chromatin detected in G1 becomes constrained in S phase through a mechanism dependent on active DNA replication. In contrast, telomeres and centromeres provide replication-independent constraint on chromatin movement in both G1 and S phases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heun, P -- Laroche, T -- Shimada, K -- Furrer, P -- Gasser, S M -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2181-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Geneva, Department of Molecular Biology, Quai Ernest-Ansermet 30, CH-1211 Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11739961" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Cell Nucleus/physiology ; Centromere/physiology ; Chromatin/*physiology ; Chromosomes, Fungal/*physiology ; DNA Replication ; DNA, Fungal/biosynthesis ; G1 Phase ; Green Fluorescent Proteins ; *Interphase ; Luminescent Proteins ; Motion Pictures as Topic ; Mutation ; Nuclear Envelope/physiology ; Replication Origin ; S Phase ; Saccharomyces cerevisiae/genetics/growth & development/*physiology ; Telomere/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A sense of the end (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-29
    Description: How a cell distinguishes a double-strand break from the end of a chromosome has long fascinated cell biologists. It was thought that the protection of chromosomal ends required either a telomere-specific complex or the looping back of the 3' TG-rich overhang to anneal with a homologous double-stranded repeat. These models must now accommodate the findings that complexes involved in nonhomologous end joining play important roles in normal telomere length maintenance, and that subtelomeric chromatin changes in response to the DNA damage checkpoint. A hypothetical chromatin assembly checkpoint may help to explain why telomeres and the double-strand break repair machinery share essential components.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gasser, S M -- New York, N.Y. -- Science. 2000 May 26;288(5470):1377-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland. sgasser@eliot.unil.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827940" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Nuclear ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; DNA/metabolism ; DNA Damage ; *DNA Helicases ; *DNA Repair ; DNA Replication ; DNA-Binding Proteins/metabolism ; Humans ; Nuclear Proteins/metabolism ; *Proteins ; *Ribonucleases ; *Saccharomyces cerevisiae Proteins ; Telomerase/metabolism ; Telomere/*chemistry/*metabolism ; Transcription Factors/metabolism ; Yeasts/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Visualizing chromatin dynamics in interphase nuclei (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: Real-time fluorescence microscopy has emerged as a powerful tool for examining chromatin dynamics. The initial lesson is that much of the genome, particularly in yeast, is highly dynamic. Its movement within the interphase nucleus is correlated with metabolic activity. Nonetheless, the nucleus is an organelle with conserved rules of organization. Determining the distribution and regulation of mobile domains in interphase chromosomes, and characterizing sites of anchorage, will undoubtedly shed new light on the function of nuclear order.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gasser, Susan M -- New York, N.Y. -- Science. 2002 May 24;296(5572):1412-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Geneva, Quai Ernest-Ansermet 30, CH-1211 Geneva, Switzerland. susan.gasser@molbio.unige.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029120" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/physiology/*ultrastructure ; Centromere/physiology/ultrastructure ; Chromatin/*physiology/*ultrastructure ; Chromosomes/*physiology/ultrastructure ; DNA/genetics/metabolism ; Drosophila ; Gene Expression Regulation ; *Interphase ; Microscopy, Confocal ; Microscopy, Fluorescence ; Nuclear Envelope/metabolism/ultrastructure ; Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae ; Telomere/physiology/ultrastructure ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Leap year: Rare day to highlight rare diseases (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gasser, Susan M -- Lupski, James R -- Le Cam, Yann -- Menzel, Olivier -- England -- Nature. 2012 Jan 18;481(7381):265. doi: 10.1038/481265a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22258596" target="_blank"〉PubMed〈/a〉
    Keywords: Biomedical Research/economics ; *Congresses as Topic ; Humans ; International Cooperation ; *Rare Diseases/epidemiology ; Switzerland
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-10-25
    Description: Recent findings suggest important roles for nuclear organization in gene expression. In contrast, little is known about how nuclear organization contributes to genome stability. Epistasis analysis (E-MAP) using DNA repair factors in yeast indicated a functional relationship between a nuclear pore subcomplex and Slx5/Slx8, a small ubiquitin-like modifier (SUMO)-dependent ubiquitin ligase, which we show physically interact. Real-time imaging and chromatin immunoprecipitation confirmed stable recruitment of damaged DNA to nuclear pores. Relocation required the Nup84 complex and Mec1/Tel1 kinases. Spontaneous gene conversion can be enhanced in a Slx8- and Nup84-dependent manner by tethering donor sites at the nuclear periphery. This suggests that strand breaks are shunted to nuclear pores for a repair pathway controlled by a conserved SUMO-dependent E3 ligase.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518492/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518492/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nagai, Shigeki -- Dubrana, Karine -- Tsai-Pflugfelder, Monika -- Davidson, Marta B -- Roberts, Tania M -- Brown, Grant W -- Varela, Elisa -- Hediger, Florence -- Gasser, Susan M -- Krogan, Nevan J -- R01 GM084448/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Oct 24;322(5901):597-602. doi: 10.1126/science.1162790.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18948542" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin Immunoprecipitation ; *DNA Breaks, Double-Stranded ; DNA Repair ; DNA, Fungal/genetics/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Deoxyribonucleases, Type II Site-Specific/metabolism ; Gene Conversion ; Genes, Fungal ; Immunoprecipitation ; Intracellular Signaling Peptides and Proteins/metabolism ; Kinetics ; Nuclear Pore/*metabolism ; Nuclear Pore Complex Proteins/genetics/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombination, Genetic ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Ubiquitin-Protein Ligases/*metabolism ; Zinc Fingers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
    Electronic Resource
    Electronic Resource
    Reactively sputtered Ru–Si–O films (1999)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 86 (1999), S. 1974-1981 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Films of Ru–Si–O were synthesized by reactively sputtering a Ru1Si1 target in an Ar/O2 gas mixture. They were characterized in terms of their composition by 2.0 MeV 4He++ backscattering spectrometry, their atomic density by thickness measurements combined with backscattering data, their microstructure by x-ray diffraction and transmission electron microscopy, and their electrical resistivity by four-point-probe measurements. The compositions indicate preferential sputtering with ruthenium enrichment of the films, and a saturation level of oxygen is determined at 67 at. % corresponding to the formation of SiO2 and RuO2. X-ray diffraction spectra reveal an amorphous structure for oxygen-saturated and nanocrystals for unsaturated as-deposited films. The crystallization temperature clearly increases with the oxygen concentration of the films, from 500 °C for oxygen-free films to 1000 °C for oxygen-saturated films, when annealed in vacuum for 30 min. Transmission electron micrographs of as-deposited oxygen-saturated films show few nanocrystals of 1–2 nm in diameter in an otherwise amorphous matrix. The atomic density is roughly 8×1022 atom/cm3 for all compositions. The resistivity of the ternary alloys scales with the terminal phases in the ternary phase diagram and reaches a maximum value when the Ru–SiO2 tie line is crossed near 50 at. % oxygen. The films are stable in vacuum up to thermal stressing at 800 °C for 5 h, and their decomposition starts near 1000 °C. © 1999 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.370996
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  • 7
    Electronic Resource
    Electronic Resource
    Nuclear organization and transcriptional silencing in yeast (1996)
    Springer
    Cellular and molecular life sciences 52 (1996), S. 1136-1147 
    Details
    ISSN: 1420-9071
    Keywords: Silencing ; Sir ; yeast mating type ; telomere position effect ; subnuclear organization ; chromatin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Transcriptional repression at the yeast silent mating type loci requires the formation of a nucleoprotein complex at specific cis-acting elements called silencers, which in turn promotes the binding of a histone-associated Sir-protein complex to adjacent chromatin. A similar mechanism of long-range transcriptional repression appears to function near telomeric repeat sequences, where it has been demonstrated that Sir3p is a limiting factor for the propagation of silencing. A combined immunofluorescence/in situ hybridization method for budding yeast was developed that maintains the three-dimensional structure of the nucleus. In wild-type cells the immunostaining of Sir3p, Sir4p and Rap1 colocalizes with Y′ subtelomeric sequences detected by in situ hybridization. All three antigens and the subtelomeric in situ hybridization signals are clustered in foci, which are often adjacent to, but not coincident with, nuclear pores. This colocalization of Rap1, Sir3p and Sir4p with telomeres is lost insir mutants, and also when Sir4p is overexpressed. To test whether the natural positioning of the twoHM loci, located roughly 10 and 25 kb from the ends of chromosome III, is important for silencer function, a reporter gene flanked by wild-type silencer elements was integrated at various internal sites on other yeast chromosomes. We find that integration at internal loci situated far from telomeres abrogates the ability of silencers to repress the reporter gene. Silencing can be restored by creation of a telomere at 13 kb from the reporter construct, or by insertion of 340 bp of yeast telomeric repeat sequence at this site without chromosomal truncation. Elevation of the internal nuclear pools of Sir1p, Sir3p and Sir4p can relieve the lack of repression at theLYS2 locus in an additive manner, suggesting that in wild-type cells silencer function is facilitated by its juxtaposition to a pool of highly concentrated Sir proteins, such as those created by telomere clustering.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01952113
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  • 8
    Electronic Resource
    Electronic Resource
    Multi-author Review¶Epigenetic control of transcription¶Introduction: the genetics of epigenetics (1998)
    Springer
    Cellular and molecular life sciences 54 (1998), S. 1-5 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Epigenetics; chromatin; transcription; silencing; acetylation; dosage compensation; methylation; paramutation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Cis-acting binding sites for transcription activators cannot explain the patterned expression of genes during development, nor a large range of phenomena that result from gene transplacement. Heritable states of transcriptional regression or activation sequences are influenced not only by the chromosomal context of the promoter but also by modifications of histones and DNA, and long-range interactions between distant chromosomal elements. The molecular dissection of these epigenetic phenomena has become an exciting topic of reserch, revealing highly conserved mechanisms at work in chromatin-mediated gene control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050120
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  • 9
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    Imported mitochondrial proteins cytochrome b2 and cytochrome c1 are processed in two steps. (1982)
    National Academy of Sciences
    Details
    Publication Date: 1982-01-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Long-range compaction and flexibility of interphase chromatin in budding yeast analyzed by high-resolution imaging techniques (2004)
    National Academy of Sciences
    Details
    Publication Date: 2004-11-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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